ID   SYI_META3               Reviewed;        1040 AA.
AC   A6UVK2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02003};
DE            EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02003};
DE   AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02003};
DE            Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02003};
GN   Name=ileS {ECO:0000255|HAMAP-Rule:MF_02003}; OrderedLocusNames=Maeo_0945;
OS   Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS   Nankai-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=419665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus aeolicus Nankai-3.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS
CC       can inadvertently accommodate and process structurally similar amino
CC       acids such as valine, to avoid such errors it has two additional
CC       distinct tRNA(Ile)-dependent editing activities. One activity is
CC       designated as 'pretransfer' editing and involves the hydrolysis of
CC       activated Val-AMP. The other activity is designated 'posttransfer'
CC       editing and involves deacylation of mischarged Val-tRNA(Ile).
CC       {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-
CC         isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666,
CC         Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528,
CC         ChEBI:CHEBI:456215; EC=6.1.1.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02003};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02003};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- DOMAIN: IleRS has two distinct active sites: one for aminoacylation and
CC       one for editing. The misactivated valine is translocated from the
CC       active site to the editing site, which sterically excludes the
CC       correctly activated isoleucine. The single editing site contains two
CC       valyl binding pockets, one specific for each substrate (Val-AMP or Val-
CC       tRNA(Ile)). {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       IleS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02003}.
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DR   EMBL; CP000743; ABR56524.1; -; Genomic_DNA.
DR   RefSeq; WP_011973656.1; NC_009635.1.
DR   AlphaFoldDB; A6UVK2; -.
DR   SMR; A6UVK2; -.
DR   STRING; 419665.Maeo_0945; -.
DR   EnsemblBacteria; ABR56524; ABR56524; Maeo_0945.
DR   GeneID; 5327661; -.
DR   KEGG; mae:Maeo_0945; -.
DR   eggNOG; arCOG00807; Archaea.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 4914at2157; -.
DR   Proteomes; UP000001106; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033709; Anticodon_Ile_ABEc.
DR   InterPro; IPR002301; Ile-tRNA-ligase.
DR   InterPro; IPR023586; Ile-tRNA-ligase_type2.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   PANTHER; PTHR42780; PTHR42780; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00392; ileS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..1040
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_1000022150"
FT   MOTIF           47..57
FT                   /note="'HIGH' region"
FT   MOTIF           605..609
FT                   /note="'KMSKS' region"
FT   BINDING         608
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1040 AA;  121325 MW;  21BA4C114FCB46B2 CRC64;
     MKEIKGKVDF REMDKEIKEF WENNEIYQKV KKLNENYPDY YFVDGPPYCS GSIHLGTAWN
     KTIKDTVLRF KRMQNYNVLD KAGWDMHGLP IEVKVEHEFN LQSKKDIETK VGTDVFIEKC
     KEFALNNKEV MENQFKNLGI WLDWENAYLP IKNDYIEAGW WSLKRAHEKE LLSKDLRVGY
     WCPRCETSLA EHEVRGEYQD VLDPSVYVKF KVADDNSYPN TYFVIWTTTP WTLISNLLIA
     VNPEFDYGFV EVIFDNERKE TWVIAEALVE AVIKLAKKQN NIKSYNIVKK VKGKELEGIK
     YVPALLEENE RQKEFFQLEK VHTIVLGEHV SLDGGTGLVH TAPGFGEEDF EVGKKYNSPI
     YSPIDDEGKY VEGKWKGVFV KDADEDIIAT LTDKNLIVNA GKKKHTYPHC WRCKTPLLFR
     STEQWFLNIS KIKNNIVEHA KNTDWVPNWV ETRYINGVKF VGDWNISRQR YWGIPLPIWI
     CENKDCGKYK IIGSVEELKQ EMINDIPIND DLHKPTVDKI IMKCDCGCEM KRTPDVLDVW
     YDSGLAPYAS INAKELKKAD FIVEGNDQVT KWFYSQHALS EIVFDDIPYK KCMMHGFTLD
     ETGEKMSKSI GNVVNPDDVV EEFGADLLRF YLLSANKAWE DLRFSIGEMN DVKSVFNTLW
     NSYSFAVNYM VLDDFSPNEE YFNYLRDEDK WIISKINSLT KEAIEVLEIP HLHEYTWKVR
     DFILNDLSRW YIKLIRNRTW MEKEDPDKLS AYQTLYYVLM KLVVILAPVA PHISEKIYQN
     LKIEGMPQSI FMTKIVVEEE YINKEVEEGI ETAREIVDAI LKGRDKVKYT LRYPISKIIL
     PNELGDIVNK YHYIIKEQGN VKNIEVKEFE GNISLKPNFR TLGASFKSDV PAVVKILNSQ
     NPKELKDKLA EGEITIDGFT IKPEHVEFKI DIPDNIVGME LRKGSVYIDI ELTEEIIKDG
     LKREVIRRIQ SMRKDMDLDI EEKIKITMEG IEFNEDALKD IEKEVRGTFE PTIECDNIQE
     WNIKTPNGEV YNLKIGVKKN